Linear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A2’s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom

dc.creatorDe Simone, Salvatore Giovanni
dc.creatorPêgo, Paloma Napoleão
dc.creatorPinto, Luiz André Lucas Teixeira
dc.creatorSantos, Jonathas D. L.
dc.creatorSimone, Thatiane S. De
dc.creatorMelgarejo Gimenez, Anibal Rafael
dc.creatorAguiar, Aniesse S.
dc.creatorSalvador, Daniela P. Marchi
dc.date2015-08-19T13:49:29Z
dc.date2015-08-19T13:49:29Z
dc.date2013
dc.date.accessioned2023-09-26T23:59:11Z
dc.date.available2023-09-26T23:59:11Z
dc.identifierSIMONE, Salvatore G. De; et al. Linear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A2’s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom. Toxicon, v.72, p.90–101, 2013.
dc.identifier0041-0101
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/11534
dc.identifier10.1016/j.toxicon.2013.06.004
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8896251
dc.descriptionThe benefits from treatment with antivenom sera are indubitable. However, the mechanism for toxin neutralization has not been completely elucidated. A mixture of antibothropic and anti-crotalic horse antivenom has been reported to be more effective in neutralizing the effects of Bothrops jararacussu snake venom than anti-bothropic antivenom alone. This study determined which regions in the three PLA2s from B. jararacussu snake venom are bound by antibodies in tetravalent anti-bothropic and monovalent anticrotalic commercial horse antivenom. Mapping experiments of BthTX-I, BthTX-II and BthAI using two small libraries of 69 peptides each revealed six major IgG-binding epitopes that were recognized by both anti-bothropic and anti-crotalic horse antivenom. Two epitopes in BthTX-I were only recognized by the anti-bothropic horse antivenom, while anti-crotalic horse antivenom recognized four unique epitopes across the three PLA2s. Our studies suggest that the harmful activities of the PLA2s present in the venom of B. jararacussu are neutralized by the combinatorial treatment with both antivenom sera through their complementary binding sites, which provides a wide coverage on the PLA2s. This is the first peptide microarray of PLA2s from B. jararacussu snake venom to survey the performance of commercial horse antiophidic antivenom. Regions recognized by the protective antivenom sera are prime candidates for improved venom cocktails or a chimeric protein encoding the multiple epitopes to immunize animals as well as for designing future synthetic vaccines.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectPhospholipase A2
dc.subjectPeptide array
dc.subjectSPOT-synthesis
dc.subjectSynthetic peptides
dc.subjectB-epitopes
dc.subjectAntigenic determinants
dc.subjectEpitopos
dc.subjectPeptídeos
dc.subjectLisofosfolipase
dc.titleLinear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A2’s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom
dc.typeArticle


Este ítem pertenece a la siguiente institución